PDBsum entry 1f43

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protein links
Transcription PDB id
Protein chain
61 a.a. *
* Residue conservation analysis
PDB id:
Name: Transcription
Title: Solution structure of the mata1 homeodomain
Structure: Mating-type protein a-1. Chain: a. Fragment: homeodomain, c-terminal domain (66-126). Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: J.S.Anderson,M.Forman,S.Modleski,F.W.Dahlquist,S.M.Baxter
Key ref:
J.S.Anderson et al. (2000). Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain. Biochemistry, 39, 10045-10054. PubMed id: 10955992 DOI: 10.1021/bi000677z
07-Jun-00     Release date:   26-Jul-00    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P0CY10  (MATA1_YEASX) -  Mating-type protein A1
126 a.a.
61 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     regulation of transcription, DNA-dependent   1 term 
  Biochemical function     DNA binding     3 terms  


DOI no: 10.1021/bi000677z Biochemistry 39:10045-10054 (2000)
PubMed id: 10955992  
Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain.
J.S.Anderson, M.D.Forman, S.Modleski, F.W.Dahlquist, S.M.Baxter.
The mating type homeodomain proteins, MATa1 and MATalpha2, combine to form a heterodimer to bind DNA in diploid yeast cells. The a1-alpha2 heterodimer tightly and specifically binds haploid-specific gene operators to repress transcription. On its own, however, the a1 homeodomain does not bind DNA in a sequence-specific manner. To help understand this interaction, we describe the solution structure and backbone dynamics of the free a1 homeodomain. Free a1 in solution is an ensemble of structures having flexible hinges at the two turns in the small protein fold. Conformational changes in the a1 homeodomain upon ternary complex formation are located in the loop between helix 1 and helix 2, where the C-terminal tail of alpha2 binds to form the heterodimer, and at the C-terminus of helix 3, the DNA recognition helix. The observed differences, comparing the free and bound a1 structures, suggest a mechanism linking van der Waals stacking changes to the ordering of a final turn in the DNA-binding helix of a1. The tail of alpha2 induces changes in loop 1 of a1 that push it toward a properly folded DNA binding conformation.

Literature references that cite this PDB file's key reference

  PubMed id Reference
15388867 R.Schleif, and C.Wolberger (2004).
Arm-domain interactions can provide high binding cooperativity.
  Protein Sci, 13, 2829-2831.  
12538894 A.Ke, and C.Wolberger (2003).
Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera.
  Protein Sci, 12, 306-312.
PDB codes: 1mh3 1mh4
12923178 E.J.Stollar, U.Mayor, S.C.Lovell, L.Federici, S.M.Freund, A.R.Fersht, and B.F.Luisi (2003).
Crystal structures of engrailed homeodomain mutants: implications for stability and dynamics.
  J Biol Chem, 278, 43699-43708.
PDB codes: 1p7i 1p7j
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